NPM1
Gene Ontology Biological Process
- CENP-A containing nucleosome assembly [TAS]
- DNA repair [IDA]
- cell aging [IMP, ISS]
- centrosome cycle [IMP, ISS]
- intracellular protein transport [TAS]
- negative regulation of apoptotic process [IDA, NAS]
- negative regulation of cell proliferation [IMP, ISS]
- negative regulation of centrosome duplication [IMP]
- negative regulation of protein kinase activity by regulation of protein phosphorylation [IDA]
- nucleocytoplasmic transport [IDA, TAS]
- nucleosome assembly [IDA, TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of translation [IDA]
- protein localization [IDA]
- protein oligomerization [IDA]
- regulation of centriole replication [IMP]
- regulation of eIF2 alpha phosphorylation by dsRNA [IDA]
- regulation of endodeoxyribonuclease activity [IDA]
- regulation of endoribonuclease activity [IDA]
- response to stress [IMP]
- ribosome assembly [TAS]
- signal transduction [NAS]
- viral process [TAS]
Gene Ontology Molecular Function- NF-kappaB binding [IDA, ISS]
- RNA binding [IDA]
- Tat protein binding [IDA]
- histone binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IMP]
- protein homodimerization activity [IDA]
- protein kinase binding [IPI]
- protein kinase inhibitor activity [IDA]
- ribosomal large subunit binding [IDA]
- ribosomal small subunit binding [IDA]
- transcription coactivator activity [IDA]
- unfolded protein binding [IDA, ISS]
- NF-kappaB binding [IDA, ISS]
- RNA binding [IDA]
- Tat protein binding [IDA]
- histone binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IMP]
- protein homodimerization activity [IDA]
- protein kinase binding [IPI]
- protein kinase inhibitor activity [IDA]
- ribosomal large subunit binding [IDA]
- ribosomal small subunit binding [IDA]
- transcription coactivator activity [IDA]
- unfolded protein binding [IDA, ISS]
Gene Ontology Cellular Component
CHEK1
Gene Ontology Biological Process
- DNA damage checkpoint [IDA, IMP]
- DNA damage induced protein phosphorylation [IDA]
- DNA repair [IMP]
- DNA replication [TAS]
- G2 DNA damage checkpoint [IMP]
- cellular response to DNA damage stimulus [IMP]
- cellular response to mechanical stimulus [IEP]
- chromatin-mediated maintenance of transcription [ISS]
- negative regulation of mitosis [IDA]
- peptidyl-threonine phosphorylation [IDA]
- regulation of double-strand break repair via homologous recombination [IDA]
- regulation of histone H3-K9 acetylation [ISS]
- regulation of mitotic centrosome separation [IDA]
- regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage [ISS]
- replicative senescence [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Interaction with checkpoint kinase 1 modulates the recruitment of nucleophosmin to chromatin.
The Checkpoint kinase 1 (Chk1) plays a central role in the cellular response to DNA damage and also contributes to the efficacy of DNA replication in the absence of genomic stress. However, we have only limited knowledge regarding the molecular mechanisms that regulate differential Chk1 function in the absence and presence of DNA damage. To address this, we used vertebrate ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CHEK1 NPM1 | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| NPM1 CHEK1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| CHEK1 NPM1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID